Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-1-24
pubmed:databankReference
pubmed:abstractText
We purified a new EF-hand type calcium binding protein from chicken gizzard smooth muscle, tentatively named calgizzarin (Todoroki, H., et al. J. Biol. Chem. (1991) in press. Based on the internal peptide sequence of calgizzarin, we isolated and sequenced a cDNA clone coding for calgizzarin from a rabbit lung cDNA library. This clone (pCALG) has 309 nucleotides of open reading frame including termination codon TGA, 621 nucleotides of the 5' leader and 186 nucleotides of the 3' noncoding region. The polypeptides deduced from the open reading frame were consisted of 102 amino acid residues with a molecular weight of 11,429. Computer aided homology analysis revealed that calgizzarin exhibits a 43.2% homology to S-100 alpha, 38.6% to S-100 beta and 40.0% to annexin II light chain, p10. By Northern blot analysis, with pCALG, a band of 1.1 kbp was detected in rabbit lung, suggesting pCALG contains nearly full length of mRNA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
181
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
644-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Molecular cloning and sequencing of a cDNA clone encoding a new calcium binding protein, named calgizzarin, from rabbit lung.
pubmed:affiliation
Department of Pharmacology, Nagoya University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't